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Conserved domains on  [gi|193210500|ref|NP_510166|]
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TBPIP domain-containing protein [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
E2F_DD super family cl22411
Dimerization domain of E2F transcription factors; E2F transcription factors are involved in ...
259-317 1.23e-05

Dimerization domain of E2F transcription factors; E2F transcription factors are involved in the regulation of DNA synthesis, cell cycle progression, proliferation and apoptosis. It associates with the retinoblastoma (Rb) protein, negatively regulating the G1-S transition until cyclin-dependent kinases phosphorylate Rb, which causes E2F release. E2F forms heterodimers with DP, a distantly related protein. Heterodimerization enhances the Rb binding, DNA binding, and transactivation activities of E2Fs. In humans, there are at least six closely related E2F and two DP family members, all containing a DNA-binding domain, a coiled-coil (CC) region, and a marked-box domain. E2F1 to E2F5 also contain a C-terminal transactivation domain.


The actual alignment was detected with superfamily member cd14660:

Pssm-ID: 473951 [Multi-domain]  Cd Length: 104  Bit Score: 44.43  E-value: 1.23e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193210500 259 DEFQSTHIEIEKLDQEEKELDEMLEIAQKQLAEVKRNP----YAFFTSADI----NLRGNEVLIAKA 317
Cdd:cd14660    1 DRLSKLKEEIEELEAEEKELDELIRWCQQSLKNLTEDPenqkLAYVTYEDIrsipSFKEQTVIAIKA 67
PTZ00108 super family cl36510
DNA topoisomerase 2-like protein; Provisional
254-515 7.84e-05

DNA topoisomerase 2-like protein; Provisional


The actual alignment was detected with superfamily member PTZ00108:

Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 46.19  E-value: 7.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210500  254 KFKEIDEFQSTHIE---IEKLDQEEKELDEMLEIAQKQLAEVKRNPYAFFTSADINLRGNEVLIAKAhdvtvdcmtgmnr 330
Cdd:PTZ00108 1114 KEKELEKLKNTTPKdmwLEDLDKFEEALEEQEEVEEKEIAKEQRLKSKTKGKASKLRKPKLKKKEKK------------- 1180
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210500  331 vVTNMDAVKIDKMNYLNNRFP--KEALTKIDNKKYKAAAKIIDKNIGQDKVQLKQ--KSKDEAVMKILRQFSGTNEASDP 406
Cdd:PTZ00108 1181 -KKKSSADKSKKASVVGNSKRvdSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKpkKSSVKRLKSKKNNSSKSSEDNDE 1259
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210500  407 SDERPVHQ-ALGINKKMAHQTTQNSQLRITT------SGNELKVSIGKKFDEAQINKLQTEKELKKNA-QKQANAAKMRE 478
Cdd:PTZ00108 1260 FSSDDLSKeGKPKNAPKRVSAVQYSPPPPSKrpdgesNGGSKPSSPTKKKVKKRLEGSLAALKKKKKSeKKTARKKKSKT 1339
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 193210500  479 KRAKAKEEQEGSRARKRKNTdeptlpiKRQDSIDSEC 515
Cdd:PTZ00108 1340 RVKQASASQSSRLLRRPRKK-------KSDSSSEDDD 1369
 
Name Accession Description Interval E-value
E2F_DD cd14660
Dimerization domain of E2F transcription factors; E2F transcription factors are involved in ...
259-317 1.23e-05

Dimerization domain of E2F transcription factors; E2F transcription factors are involved in the regulation of DNA synthesis, cell cycle progression, proliferation and apoptosis. It associates with the retinoblastoma (Rb) protein, negatively regulating the G1-S transition until cyclin-dependent kinases phosphorylate Rb, which causes E2F release. E2F forms heterodimers with DP, a distantly related protein. Heterodimerization enhances the Rb binding, DNA binding, and transactivation activities of E2Fs. In humans, there are at least six closely related E2F and two DP family members, all containing a DNA-binding domain, a coiled-coil (CC) region, and a marked-box domain. E2F1 to E2F5 also contain a C-terminal transactivation domain.


Pssm-ID: 271137 [Multi-domain]  Cd Length: 104  Bit Score: 44.43  E-value: 1.23e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193210500 259 DEFQSTHIEIEKLDQEEKELDEMLEIAQKQLAEVKRNP----YAFFTSADI----NLRGNEVLIAKA 317
Cdd:cd14660    1 DRLSKLKEEIEELEAEEKELDELIRWCQQSLKNLTEDPenqkLAYVTYEDIrsipSFKEQTVIAIKA 67
E2F_CC-MB pfam16421
E2F transcription factor CC-MB domain; This is the coiled coil (CC) - marked box (MB) domain ...
267-317 4.87e-05

E2F transcription factor CC-MB domain; This is the coiled coil (CC) - marked box (MB) domain of E2F transcription factors. This domain forms a heterodimer with the corresponding domain of the DP transcription factor, the heterodimer binds the C-terminus of retinoblastoma protein.


Pssm-ID: 465115  Cd Length: 96  Bit Score: 42.57  E-value: 4.87e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 193210500  267 EIEKLDQEEKELDEMLEIAQKQLAEV----KRNPYAFFTSADI----NLRGNEVLIAKA 317
Cdd:pfam16421   4 ELEDLEEEEEELDQLIRWLQQSLKNLtedeKNQKLAYVTYQDIrsipCFQEQTVIAIKA 62
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
254-515 7.84e-05

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 46.19  E-value: 7.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210500  254 KFKEIDEFQSTHIE---IEKLDQEEKELDEMLEIAQKQLAEVKRNPYAFFTSADINLRGNEVLIAKAhdvtvdcmtgmnr 330
Cdd:PTZ00108 1114 KEKELEKLKNTTPKdmwLEDLDKFEEALEEQEEVEEKEIAKEQRLKSKTKGKASKLRKPKLKKKEKK------------- 1180
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210500  331 vVTNMDAVKIDKMNYLNNRFP--KEALTKIDNKKYKAAAKIIDKNIGQDKVQLKQ--KSKDEAVMKILRQFSGTNEASDP 406
Cdd:PTZ00108 1181 -KKKSSADKSKKASVVGNSKRvdSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKpkKSSVKRLKSKKNNSSKSSEDNDE 1259
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210500  407 SDERPVHQ-ALGINKKMAHQTTQNSQLRITT------SGNELKVSIGKKFDEAQINKLQTEKELKKNA-QKQANAAKMRE 478
Cdd:PTZ00108 1260 FSSDDLSKeGKPKNAPKRVSAVQYSPPPPSKrpdgesNGGSKPSSPTKKKVKKRLEGSLAALKKKKKSeKKTARKKKSKT 1339
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 193210500  479 KRAKAKEEQEGSRARKRKNTdeptlpiKRQDSIDSEC 515
Cdd:PTZ00108 1340 RVKQASASQSSRLLRRPRKK-------KSDSSSEDDD 1369
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
226-317 9.27e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 39.53  E-value: 9.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210500 226 LNMVVRRLEELGAIERPLNLHVRFTPEFKFKEIDEFQS----THIEIEK----LDQEEKELDEMLEIAQKQLAEVKrnPY 297
Cdd:PRK05771  52 LTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKdveeELEKIEKeikeLEEEISELENEIKELEQEIERLE--PW 129
                         90       100
                 ....*....|....*....|
gi 193210500 298 AFFTSADINLRGNEVLIAKA 317
Cdd:PRK05771 130 GNFDLDLSLLLGFKYVSVFV 149
 
Name Accession Description Interval E-value
E2F_DD cd14660
Dimerization domain of E2F transcription factors; E2F transcription factors are involved in ...
259-317 1.23e-05

Dimerization domain of E2F transcription factors; E2F transcription factors are involved in the regulation of DNA synthesis, cell cycle progression, proliferation and apoptosis. It associates with the retinoblastoma (Rb) protein, negatively regulating the G1-S transition until cyclin-dependent kinases phosphorylate Rb, which causes E2F release. E2F forms heterodimers with DP, a distantly related protein. Heterodimerization enhances the Rb binding, DNA binding, and transactivation activities of E2Fs. In humans, there are at least six closely related E2F and two DP family members, all containing a DNA-binding domain, a coiled-coil (CC) region, and a marked-box domain. E2F1 to E2F5 also contain a C-terminal transactivation domain.


Pssm-ID: 271137 [Multi-domain]  Cd Length: 104  Bit Score: 44.43  E-value: 1.23e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193210500 259 DEFQSTHIEIEKLDQEEKELDEMLEIAQKQLAEVKRNP----YAFFTSADI----NLRGNEVLIAKA 317
Cdd:cd14660    1 DRLSKLKEEIEELEAEEKELDELIRWCQQSLKNLTEDPenqkLAYVTYEDIrsipSFKEQTVIAIKA 67
E2F_CC-MB pfam16421
E2F transcription factor CC-MB domain; This is the coiled coil (CC) - marked box (MB) domain ...
267-317 4.87e-05

E2F transcription factor CC-MB domain; This is the coiled coil (CC) - marked box (MB) domain of E2F transcription factors. This domain forms a heterodimer with the corresponding domain of the DP transcription factor, the heterodimer binds the C-terminus of retinoblastoma protein.


Pssm-ID: 465115  Cd Length: 96  Bit Score: 42.57  E-value: 4.87e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 193210500  267 EIEKLDQEEKELDEMLEIAQKQLAEV----KRNPYAFFTSADI----NLRGNEVLIAKA 317
Cdd:pfam16421   4 ELEDLEEEEEELDQLIRWLQQSLKNLtedeKNQKLAYVTYQDIrsipCFQEQTVIAIKA 62
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
254-515 7.84e-05

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 46.19  E-value: 7.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210500  254 KFKEIDEFQSTHIE---IEKLDQEEKELDEMLEIAQKQLAEVKRNPYAFFTSADINLRGNEVLIAKAhdvtvdcmtgmnr 330
Cdd:PTZ00108 1114 KEKELEKLKNTTPKdmwLEDLDKFEEALEEQEEVEEKEIAKEQRLKSKTKGKASKLRKPKLKKKEKK------------- 1180
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210500  331 vVTNMDAVKIDKMNYLNNRFP--KEALTKIDNKKYKAAAKIIDKNIGQDKVQLKQ--KSKDEAVMKILRQFSGTNEASDP 406
Cdd:PTZ00108 1181 -KKKSSADKSKKASVVGNSKRvdSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKpkKSSVKRLKSKKNNSSKSSEDNDE 1259
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210500  407 SDERPVHQ-ALGINKKMAHQTTQNSQLRITT------SGNELKVSIGKKFDEAQINKLQTEKELKKNA-QKQANAAKMRE 478
Cdd:PTZ00108 1260 FSSDDLSKeGKPKNAPKRVSAVQYSPPPPSKrpdgesNGGSKPSSPTKKKVKKRLEGSLAALKKKKKSeKKTARKKKSKT 1339
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 193210500  479 KRAKAKEEQEGSRARKRKNTdeptlpiKRQDSIDSEC 515
Cdd:PTZ00108 1340 RVKQASASQSSRLLRRPRKK-------KSDSSSEDDD 1369
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
226-317 9.27e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 39.53  E-value: 9.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210500 226 LNMVVRRLEELGAIERPLNLHVRFTPEFKFKEIDEFQS----THIEIEK----LDQEEKELDEMLEIAQKQLAEVKrnPY 297
Cdd:PRK05771  52 LTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKdveeELEKIEKeikeLEEEISELENEIKELEQEIERLE--PW 129
                         90       100
                 ....*....|....*....|
gi 193210500 298 AFFTSADINLRGNEVLIAKA 317
Cdd:PRK05771 130 GNFDLDLSLLLGFKYVSVFV 149
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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